Publication Date:
1998-05-02
Description:
The splicing of transfer RNA precursors is similar in Eucarya and Archaea. In both kingdoms an endonuclease recognizes the splice sites and releases the intron, but the mechanism of splice site recognition is different in each kingdom. The crystal structure of the endonuclease from the archaeon Methanococcus jannaschii was determined to a resolution of 2.3 angstroms. The structure indicates that the cleavage reaction is similar to that of ribonuclease A and the arrangement of the active sites is conserved between the archaeal and eucaryal enzymes. These results suggest an evolutionary pathway for splice site recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, H -- Trotta, C R -- Abelson, J -- F32 GM188930-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Apr 10;280(5361):279-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, Mail Code 147-75, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9535656" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Binding Sites
;
Catalysis
;
Cloning, Molecular
;
Crystallography, X-Ray
;
Dimerization
;
Endoribonucleases/*chemistry/genetics/metabolism
;
*Evolution, Molecular
;
HIV Long Terminal Repeat
;
Hydrogen Bonding
;
Methanococcus/*enzymology/genetics
;
Models, Molecular
;
Molecular Sequence Data
;
*Protein Conformation
;
Protein Folding
;
Protein Structure, Secondary
;
RNA Precursors/chemistry/metabolism
;
*RNA Splicing
;
RNA, Archaeal/chemistry/metabolism
;
Saccharomyces cerevisiae/enzymology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
